ALF_DICDI
ID ALF_DICDI Reviewed; 357 AA.
AC Q86A67; Q556D6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE Short=ALDO;
DE EC=4.1.2.13;
GN Name=fba; ORFNames=DDB_G0274375;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000012; EAL70080.1; -; Genomic_DNA.
DR RefSeq; XP_643874.1; XM_638782.1.
DR AlphaFoldDB; Q86A67; -.
DR SMR; Q86A67; -.
DR STRING; 44689.DDB0231387; -.
DR PaxDb; Q86A67; -.
DR EnsemblProtists; EAL70080; EAL70080; DDB_G0274375.
DR GeneID; 8619300; -.
DR KEGG; ddi:DDB_G0274375; -.
DR dictyBase; DDB_G0274375; fba.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; Q86A67; -.
DR OMA; DYREMLF; -.
DR PhylomeDB; Q86A67; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-70171; Glycolysis.
DR Reactome; R-DDI-70263; Gluconeogenesis.
DR Reactome; R-DDI-70350; Fructose catabolism.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:Q86A67; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:dictyBase.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; ISS:dictyBase.
DR GO; GO:0006096; P:glycolytic process; ISS:dictyBase.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..357
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000327835"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 38903 MW; C6906B8DBB8CCF19 CRC64;
MNSKFADELI ATAKAIVAPG KGILAADEST NTIGARFKKI NLENNEENRR AYRELLIGTG
NGVNEFIGGI ILYEETLYQK MADGRLFTDV LREQKIHIGI KVDKGVVPIP GTDGETSTQG
LDGLAERCKK YYEAGARFAK WRAVLKIDLA KNCPSQLSIT ENAHTLARYA AICQENGLVP
IVEPEILMDG NHTVEQSAEV TEKVLAAVFK ALNDHHILLE GALLKPNMVV NGTDCPIKAT
SEQIGKFTVR TLQRTVPPAL TGVVFLSGGQ TEIEATANLN AMNVLPNRPW ALSFSYGRAL
QASVISTWKG ESANVEAARK VYLHRAKCNS LAQLGKYTGE ESTGSASESL YVKDYKY